ID   ATGT_PICTO              Reviewed;         625 AA.
AC   Q6L1W3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
DE            EC=2.4.2.48 {ECO:0000255|HAMAP-Rule:MF_01634};
DE   AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01634};
DE   AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
GN   Name=tgtA {ECO:0000255|HAMAP-Rule:MF_01634}; OrderedLocusNames=PTO0454;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine
CC       (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal
CC       tRNAs. {ECO:0000255|HAMAP-Rule:MF_01634}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-
CC         carbaguanosine(15) in tRNA + guanine; Xref=Rhea:RHEA:43164,
CC         Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:10372, ChEBI:CHEBI:16235,
CC         ChEBI:CHEBI:45075, ChEBI:CHEBI:74269, ChEBI:CHEBI:82850; EC=2.4.2.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01634};
CC   -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01634}.
CC   -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01634}.
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DR   EMBL; AE017261; AAT43039.1; -; Genomic_DNA.
DR   RefSeq; WP_011177255.1; NC_005877.1.
DR   AlphaFoldDB; Q6L1W3; -.
DR   SMR; Q6L1W3; -.
DR   STRING; 263820.PTO0454; -.
DR   EnsemblBacteria; AAT43039; AAT43039; PTO0454.
DR   GeneID; 2844755; -.
DR   KEGG; pto:PTO0454; -.
DR   PATRIC; fig|263820.9.peg.479; -.
DR   eggNOG; arCOG00989; Archaea.
DR   eggNOG; arCOG00991; Archaea.
DR   HOGENOM; CLU_030083_0_0_2; -.
DR   OMA; FPCSCPV; -.
DR   OrthoDB; 10236at2157; -.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.10.450.90; -; 1.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_01634; TgtA_arch; 1.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR029402; TGT_C2.
DR   InterPro; IPR038250; TGT_C2_sf.
DR   InterPro; IPR004804; TgtA.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01472; PUA; 1.
DR   Pfam; PF01702; TGT; 1.
DR   Pfam; PF14810; TGT_C2; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Metal-binding; Reference proteome; Transferase;
KW   tRNA processing; Zinc.
FT   CHAIN           1..625
FT                   /note="tRNA-guanine(15) transglycosylase"
FT                   /id="PRO_0000247880"
FT   DOMAIN          546..621
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ   SEQUENCE   625 AA;  72063 MW;  BADC42E6CFFACD0B CRC64;
     MEILFRENLA RIARFKTPHG EIETPTVMPV INPNLNFLDE STLRSYGVQA VITNSYIIKR
     NQRLNEDALR HGLHSLIKFS GPIMTDSGTF QSHVYGDIEY SNKEIVDFQK AIGSDIITIL
     DVFTEPDESY NSARSKVIET YKRLKEIDFE DKIIAGPVQG SIYPDLRRLS AYLMSDALYL
     PIGGVVPLLE SYRYSDLVKI IFNSKVSSDF SRPVHLFGGG HPMFFAFAVM LGVDLFDSAS
     YIKYAKDNRL LYSEGTRALN DIREFPEWSP IHGKYTPQEL LHEESEKRTR MLALHNLKSI
     FIEINEIKER IYENTLYNYV EEKARSHPAL FKAFMSMINY DTSDYSPLSY KSPFFYYDKT
     SLNHPIIKRI MKFTENYISN SRHTLIISSK YWRPGVKNEN VIKNIVECTD FNLLVSWNGI
     YIPLFLEDSY PVQQLVSSGL NDKKLEEDYL KRLKSINNDI EFYEGEHYDK RLRDYDTEKI
     NTIAMFQFNI NERFFDKSNI IKSKSTGHIR NIIEDNNIIA TMRNDGYLTL SIKGAYRLLS
     MKPWPGLRVV VDDESGRFNA NGYNVFFKFI KSFDTGIIPG NETLVVSEDD DLYAVGKAAV
     SGIEMYYYKS GVAVKVHEGV NKKAA